Cluster organization of the genes of Streptomyces pristinaespiralis involved in pristinamycin biosynthesis and resistance elucidated by pulsed-field gel electrophoresis

Bamas‐Jacques, Nathalie; Lorenzon, Sophie; Lacroix, Patricia; Swetschin, C. De; Crouzet, J

doi:10.1046/j.1365-2672.1999.00955.x

Cited by 30 publications

(39 citation statements)

References 31 publications

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“…The reported highest yield is just over 100 mg l -1 due to these problems. Although much attention has been paid to genetic manipulations for pristinamycins production (Blanc et al 1995(Blanc et al , 1997Hopwood 1997;Bamas-Jacques et al 1999), the yield cannot reach a satisfactory level even by engineered strain without a favorable external condition. For the above reasons, removing the antibiotic simultaneously during the fermentation could be a solution.…”

Section: Introductionmentioning

confidence: 98%

Improved production of pristinamycin coupled with an adsorbent resin in fermentation by Streptomyces pristinaespiralis

et al. 2006

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Batch fermentation by Streptomyces pristinaespiralis with the addition of adsorbent resins was used to increase the production of pristinamycin. In consideration of the adsorption capacity and the desorption ability, a polymeric resin, JD-1, was finally selected. The maximum production of pristinamycin in Erlenmeyer flasks went up to 1.13 from 0.4 g l(-1), by adding 12% (w/v) resin JD-1 into the culture broth at 20 h after inoculation. In a 3 l bioreactor, pristinamycin fermentation with the addition of 12% (w/v) resin JD-1 at 20 h after inoculation reached 0.8 g l(-1), which was a 1.25-fold increase over fermentation without resin.

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Section: Introductionmentioning

confidence: 98%

Improved production of pristinamycin coupled with an adsorbent resin in fermentation by Streptomyces pristinaespiralis

et al. 2006

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“…vat genes (including vatD) are found on transposable genetic elements, where they are sometimes associated with erm genes that confer parallel resistance to streptogramin B-class compounds (37). What then is the potential for the development of new VM or dalfopristin derivatives that are insensitive to inactivation by Vat enzymes?…”

Section: Location Of the Dalfopristin And Accoa Binding Sites-inmentioning

confidence: 99%

Structural Basis of Synercid® (Quinupristin-Dalfopristin) Resistance in Gram-positive Bacterial Pathogens

Kehoe

Snidwongse

Courvalin

et al. 2003

Journal of Biological Chemistry

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Synercid®, a new semisynthetic streptogramin-derived antibiotic containing dalfopristin and quinupristin, is used in treatment of life-threatening infections caused by glycopeptide-resistant Enterococcus faecium and other bacterial pathogens. However, dissemination of genes encoding virginiamycin acetyltransferases, enzymes that confer resistance to streptogramins, threatens to limit the medical utility of the quinupristin-dalfopristin combination. Here we present structures of virginiamycin acetyltransferase D (VatD) determined at 1.8 Å resolution in the absence of ligands, at 2.8 Å resolution bound to dalfopristin, and at 3.0 Å resolution in the presence of acetyl-coenzyme A. Dalfopristin is bound by VatD in a similar conformation to that described previously for the streptogramin virginiamycin M1. However, specific interactions with the substrate are altered as a consequence of a conformational change in the pyrollidine ring that is propagated to adjacent constituents of the dalfopristin macrocycle. Inactivation of dalfopristin involves acetyl transfer from acetylcoenzyme A to the sole (O-18) hydroxy group of the antibiotic that lies close to the side chain of the strictly conserved residue, His-82. Replacement of residue 82 by alanine is accompanied by a fall in specific activity of >10 5 -fold, indicating that the imidazole moiety of His-82 is a major determinant of catalytic rate enhancement by VatD. The structure of the VatD-dalfopristin complex can be used to predict positions where further structural modification of the drug might preclude enzyme binding and thereby circumvent Synercid® resistance.

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“…Thus, BamasJacques et al (38) demonstrated that genes directing the production of pristinamycins I and II are clustered in a 200-kb region of the chromosome of S. pristinaespiralis. The finding that genes for the biosynthesis of the pristinamycin I and II components are interspersed in this cluster led Bamas-Jacques et al to suggest that the pathways to the type A and type B streptogramins coevolved in the same organism, perhaps from a common origin.…”

mentioning

confidence: 99%

Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species

Challis

Hopwood

2003

Proc. Natl. Acad. Sci. U.S.A.

544

398

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In this article we briefly review theories about the ecological roles of microbial secondary metabolites and discuss the prevalence of multiple secondary metabolite production by strains of Streptomyces, highlighting results from analysis of the recently sequenced Streptomyces coelicolor and Streptomyces avermitilis genomes. We address this question: Why is multiple secondary metabolite production in Streptomyces species so commonplace? We argue that synergy or contingency in the action of individual metabolites against biological competitors may, in some cases, be a powerful driving force for the evolution of multiple secondary metabolite production. This argument is illustrated with examples of the coproduction of synergistically acting antibiotics and contingently acting siderophores: two well-known classes of secondary metabolite. We focus, in particular, on the coproduction of ␤-lactam antibiotics and ␤-lactamase inhibitors, the coproduction of type A and type B streptogramins, and the coregulated production and independent uptake of structurally distinct siderophores by species of Streptomyces. Possible mechanisms for the evolution of multiple synergistic and contingent metabolite production in Streptomyces species are discussed. It is concluded that the production by Streptomyces species of two or more secondary metabolites that act synergistically or contingently against biological competitors may be far more common than has previously been recognized, and that synergy and contingency may be common driving forces for the evolution of multiple secondary metabolite production by these sessile saprophytes.

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Cluster organization of the genes of Streptomyces pristinaespiralis involved in pristinamycin biosynthesis and resistance elucidated by pulsed-field gel electrophoresis

Cited by 30 publications

References 31 publications

Improved production of pristinamycin coupled with an adsorbent resin in fermentation by Streptomyces pristinaespiralis

Improved production of pristinamycin coupled with an adsorbent resin in fermentation by Streptomyces pristinaespiralis

Structural Basis of Synercid® (Quinupristin-Dalfopristin) Resistance in Gram-positive Bacterial Pathogens

Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species

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